Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector

Amrita Rai; Anurag K. Singh; Nathalie Bleimling; Guido Posern; Ingrid R. Vetter; Roger S. Goody

doi:10.1038/s41467-022-31831-1

Nature Communications (Jul 2022)

Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector

Amrita Rai,
Anurag K. Singh,
Nathalie Bleimling,
Guido Posern,
Ingrid R. Vetter,
Roger S. Goody

Affiliations

Amrita Rai: Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology
Anurag K. Singh: Institute for Physiological Chemistry, Martin Luther University Halle-Wittenberg
Nathalie Bleimling: Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology
Guido Posern: Institute for Physiological Chemistry, Martin Luther University Halle-Wittenberg
Ingrid R. Vetter: Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology
Roger S. Goody: Department of Structural Biochemistry, Max Planck Institute of Molecular Physiology

DOI: https://doi.org/10.1038/s41467-022-31831-1
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 17

Abstract

Read online

Rep15 is an effector that interacts with the GTPase Rab15. Here, the authors show that Rep15 also interacts with Rab3 paralogs and Rab34, present crystal structures of Rep15:Rab complexes and find that Rep15 depletion in glioblastoma cells decreases proliferation and mobility.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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